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Title
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The three-dimensional structure of trp repressor.
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Authors
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R.W.Schevitz,
Z.Otwinowski,
A.Joachimiak,
C.L.Lawson,
P.B.Sigler.
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Ref.
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Nature, 1985,
317,
782-786.
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PubMed id
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Abstract
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The crystal structure of the Escherichia coli trp repressor has been solved to
atomic resolution. The dimeric protein has a remarkable subunit interface in
which five of each subunit's six helices are interlinked. The binding of
L-tryptophan activates the aporepressor indirectly by fixing the orientation of
the second helix of the helix-turn-helix motif and by moulding the details of
the repressor's structure near the DNA binding surface.
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